DCL1_ASPNC
ID DCL1_ASPNC Reviewed; 1525 AA.
AC A2RAF3;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 02-OCT-2007, sequence version 2.
DT 03-AUG-2022, entry version 90.
DE RecName: Full=Dicer-like protein 1;
DE Includes:
DE RecName: Full=Endoribonuclease dcl1;
DE EC=3.1.26.-;
DE Includes:
DE RecName: Full=ATP-dependent helicase dcl1;
DE EC=3.6.4.-;
GN Name=dcl1; ORFNames=An18g02950;
OS Aspergillus niger (strain CBS 513.88 / FGSC A1513).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Pezizomycotina; Eurotiomycetes;
OC Eurotiomycetidae; Eurotiales; Aspergillaceae; Aspergillus;
OC Aspergillus subgen. Circumdati.
OX NCBI_TaxID=425011;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CBS 513.88 / FGSC A1513 / ATCC MYA-4892;
RX PubMed=17259976; DOI=10.1038/nbt1282;
RA Pel H.J., de Winde J.H., Archer D.B., Dyer P.S., Hofmann G., Schaap P.J.,
RA Turner G., de Vries R.P., Albang R., Albermann K., Andersen M.R.,
RA Bendtsen J.D., Benen J.A.E., van den Berg M., Breestraat S., Caddick M.X.,
RA Contreras R., Cornell M., Coutinho P.M., Danchin E.G.J., Debets A.J.M.,
RA Dekker P., van Dijck P.W.M., van Dijk A., Dijkhuizen L., Driessen A.J.M.,
RA d'Enfert C., Geysens S., Goosen C., Groot G.S.P., de Groot P.W.J.,
RA Guillemette T., Henrissat B., Herweijer M., van den Hombergh J.P.T.W.,
RA van den Hondel C.A.M.J.J., van der Heijden R.T.J.M., van der Kaaij R.M.,
RA Klis F.M., Kools H.J., Kubicek C.P., van Kuyk P.A., Lauber J., Lu X.,
RA van der Maarel M.J.E.C., Meulenberg R., Menke H., Mortimer M.A.,
RA Nielsen J., Oliver S.G., Olsthoorn M., Pal K., van Peij N.N.M.E.,
RA Ram A.F.J., Rinas U., Roubos J.A., Sagt C.M.J., Schmoll M., Sun J.,
RA Ussery D., Varga J., Vervecken W., van de Vondervoort P.J.J., Wedler H.,
RA Woesten H.A.B., Zeng A.-P., van Ooyen A.J.J., Visser J., Stam H.;
RT "Genome sequencing and analysis of the versatile cell factory Aspergillus
RT niger CBS 513.88.";
RL Nat. Biotechnol. 25:221-231(2007).
CC -!- FUNCTION: Dicer-like endonuclease involved in cleaving double-stranded
CC RNA in the RNA interference (RNAi) pathway. Produces 21 to 25 bp dsRNAs
CC (siRNAs) which target the selective destruction of homologous RNAs
CC leading to sequence-specific suppression of gene expression, called
CC post-transcriptional gene silencing (PTGS). Part of a broad host
CC defense response against viral infection and transposons (By
CC similarity). {ECO:0000250}.
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC Name=Mn(2+); Xref=ChEBI:CHEBI:29035; Evidence={ECO:0000250};
CC -!- SIMILARITY: Belongs to the helicase family. Dicer subfamily.
CC {ECO:0000255|PROSITE-ProRule:PRU00657}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAK48679.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
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DR EMBL; AM270401; CAK48679.1; ALT_SEQ; Genomic_DNA.
DR AlphaFoldDB; A2RAF3; -.
DR SMR; A2RAF3; -.
DR PaxDb; A2RAF3; -.
DR PRIDE; A2RAF3; -.
DR EnsemblFungi; CAK48679; CAK48679; An18g02950.
DR Proteomes; UP000006706; Chromosome 8L.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:InterPro.
DR GO; GO:0004386; F:helicase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004525; F:ribonuclease III activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051607; P:defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0031047; P:gene silencing by RNA; IEA:UniProt.
DR GO; GO:0050688; P:regulation of defense response to virus; IEA:UniProtKB-KW.
DR GO; GO:0006396; P:RNA processing; IEA:InterPro.
DR CDD; cd00593; RIBOc; 2.
DR Gene3D; 1.10.1520.10; -; 2.
DR Gene3D; 3.30.160.380; -; 1.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR038248; Dicer_dimer_sf.
DR InterPro; IPR005034; Dicer_dimerisation_dom.
DR InterPro; IPR006935; Helicase/UvrB_N.
DR InterPro; IPR014001; Helicase_ATP-bd.
DR InterPro; IPR001650; Helicase_C.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR000999; RNase_III_dom.
DR InterPro; IPR036389; RNase_III_sf.
DR Pfam; PF00271; Helicase_C; 1.
DR Pfam; PF04851; ResIII; 1.
DR Pfam; PF00636; Ribonuclease_3; 2.
DR SMART; SM00487; DEXDc; 1.
DR SMART; SM00490; HELICc; 1.
DR SMART; SM00535; RIBOc; 2.
DR SUPFAM; SSF52540; SSF52540; 1.
DR SUPFAM; SSF69065; SSF69065; 2.
DR PROSITE; PS51327; DICER_DSRBF; 1.
DR PROSITE; PS51192; HELICASE_ATP_BIND_1; 1.
DR PROSITE; PS51194; HELICASE_CTER; 1.
DR PROSITE; PS00517; RNASE_3_1; 1.
DR PROSITE; PS50142; RNASE_3_2; 2.
PE 3: Inferred from homology;
KW Antiviral defense; Antiviral protein; ATP-binding; Helicase; Hydrolase;
KW Magnesium; Manganese; Metal-binding; Nucleotide-binding;
KW Reference proteome; Repeat; RNA-binding; Zinc.
FT CHAIN 1..1525
FT /note="Dicer-like protein 1"
FT /id="PRO_0000306775"
FT DOMAIN 124..305
FT /note="Helicase ATP-binding"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT DOMAIN 439..605
FT /note="Helicase C-terminal"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00542"
FT DOMAIN 641..731
FT /note="Dicer dsRNA-binding fold"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00657"
FT DOMAIN 1032..1192
FT /note="RNase III 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1243..1394
FT /note="RNase III 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00177"
FT DOMAIN 1428..1496
FT /note="DRBM"
FT REGION 37..65
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 250..253
FT /note="DEAH box"
FT BINDING 137..144
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00541"
FT BINDING 1283
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1380
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1383
FT /ligand="Mg(2+)"
FT /ligand_id="ChEBI:CHEBI:18420"
FT /evidence="ECO:0000250"
FT BINDING 1440
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1467
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1508
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT BINDING 1510
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /evidence="ECO:0000250|UniProtKB:Q09884"
FT SITE 1376
FT /note="Important for activity"
FT /evidence="ECO:0000250"
SQ SEQUENCE 1525 AA; 173497 MW; 1A8FB7B056844A69 CRC64;
MPSAHAFDMR ITSDIYKPDQ HLPMETMKVC AVTMTEDLQE DDGSSDESDN DEREDHSKTG
VSQQRITQNA KFKALLAQRA DTGPIHDVSV THDLPDAQLS TAHLVAKQDL GIGTLDPREY
QLELFERAKV QNTIAVLDTG SGKTLIAVLL LKHTLEKELN DRMEGKPHRI AFFLVDSVTL
AYQQAAVLRN NLDQSVGHFF GAMGTDLWSK SVWDQHFQKN MVIVCTAEIL NQCLLNSYIK
MSQINILIFD EAHHTKKDHP YARIIRDSYL EEVYSKRPRI FGMTASPIDT KGDIVDEATR
LEKLLDSRIA TTSNMSLLRQ VARRPVERVW SFNKLEQPFA TSLYKHLEDR FGDMACLEGI
FRFAWQASSE LGRWCSDRAW ARALADDVLP KLEGSVRKTA NSETSSNVPE SAYKEILRIT
EASEIVKSYA FSSPETFGQL SPKVQVLREE LARYFGRQTE TKCIVFTQKR YTALILAELF
QTLNIPFLRP GVLIGVRSGD LAGMNITFRQ QFISLVKFRT GEINCLFATS VAEEGLDIPD
CNLVVRFDLY QTLIQYVQSR GRARHFNSTY ASMVERGNLE HEQRLLEVQD AEMMQSFCRT
LPEDRLLYGF DHDLDTVLQK DEGNRTFRIK STGAKLTYHS ATAILARYAS SLQYEKEFSA
QVTYVVLPIN GAFVCEVILP EKSPIRGLTG SPAMKKSIAK RSAAFDTCLL LRKNKLLDDH
FNSIYHRRLP AMRNAKLAIT SKRTSQYDMI SKPSLWGRKQ GMPPKELHGT FITFLPSMQL
SHEPAPLLLF TRERLPHFPE FPIFLDDDVE TTIITTPLEK QLLLSEKEVD ALTVFTLRVF
RDVFHKTYDK EPEKMAYWLA PAKVQSSYLP SYDPRQILDW ESLTYVRDND SIPFSTNADP
ESWVDLFVFD AWDGRCRFFT VGVEHSLTPS SPPPPFVARR RHMNDVMNYC LSLSKNSRAK
FLSTCHWDQP VLRAELVRLR RNLLDKMTDT ERDVETRCFI CIEPLKVSAI PASTAFSCLA
FPAIISRIDA YLISLQGCES LNFTVKLDLA LEAFTKDSDN TDEHRAQQIH VQRGMGRNYE
RLEFLGDCFL KMATSIALFT QNPDDDEFDY HVNRMCLICN KNLFNAAVDK EIYKYIRSRG
FSRHTWYPEG LKLLQGKDHS RKATTESKHA LAEKTIADVC EALIGAALLS GGPDHRFDMA
VKAVTTLVNS PSHKAERWKD YISFYTIPKY QRRAADGAEL YLSRKIEEKL SYRFRYPTLL
GSAFTHPSYP SAWAKVPCYQ RLEFLGDSLI DMVCVEDLFA RFPDRDPQWL TEHKMAMVSN
KFLGALAVKL GLHTHLKYFS APLQSQITQY AEEIQTAEGE SEGAVDYWTV TKDPPKCLPD
MVEAYVGAVF VDSDFNFEVI ERFFRDYIKP FFEDMAIYDT FANKHPTTFL HNRLTNEFGC
VNYCLKAGEM PSIDGAPAGV LAAVIVHDVV IAEGTATSGR YAKVKASEKA LAVLDEISSA
EFQRKFRCDC RESGDSARLD IGTAI
